This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1jra
From Proteopedia
|
Crystal Structure of Erv2p
Overview
Erv2p is an FAD-dependent sulfhydryl oxidase that can promote disulfide, bond formation during protein biosynthesis in the yeast endoplasmic, reticulum. The structure of Erv2p, determined by X-ray crystallography to, 1.5 A resolution, reveals a helix-rich dimer with no global resemblance to, other known FAD-binding proteins or thiol oxidoreductases. Two pairs of, cysteine residues are required for Erv2p activity. The first, (Cys-Gly-Glu-Cys) is adjacent to the isoalloxazine ring of the FAD. The, second (Cys-Gly-Cys) is part of a flexible C-terminal segment that can, swing into the vicinity of the first cysteine pair in the opposite subunit, of the dimer and may shuttle electrons between substrate protein dithiols, and the FAD-proximal disulfide.
About this Structure
1JRA is a Single protein structure of sequence from Saccharomyces cerevisiae with FAD as ligand. Full crystallographic information is available from OCA.
Reference
A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p., Gross E, Sevier CS, Vala A, Kaiser CA, Fass D, Nat Struct Biol. 2002 Jan;9(1):61-7. PMID:11740506
Page seeded by OCA on Tue Nov 20 18:30:49 2007
Categories: Saccharomyces cerevisiae | Single protein | Fass, D. | Gross, E. | Kaiser, C.A. | Sevier, C.S. | Vala, A. | FAD | Cxxc | Fad | Helical bundle | Sulfhydryl oxidase
